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Heme-protein fission under non-denaturing conditions

Smith, M.L. (author)
Paul, Jan (author)
Ohlsson, P.I. (author)
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Hjortsberg, K. (author)
Paul, K.G. (author)
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1991-02
1991
English.
In: Proceedings of the National Academy of Sciences of the United States of America. - : Proceedings of the National Academy of Sciences. - 0027-8424 .- 1091-6490. ; 88:3, s. 882-886
  • Journal article (peer-reviewed)
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  • Slow heme transfer from horseradish peroxidases C2 and A2, cytochrome c peroxidase, chloroperoxidase, and leghemoglobins to a heme acceptor protein, apomyoglobin, has been studied under mild conditions. The reaction is best described as heme release into water followed by quick engulfment by apomyoglobin. The energetics of the activated process are large and interpreted as connected to both polypeptide motions during release and the ordering of water around the heme during solvation. The free energy required to break the iron(III)-ligand 5 (L5) bond is a minor but crucial portion of the activation free energy. Donor-acceptor protein interactions are not involved in the transfer. Fast heme release from inactive protein has also been observed. Apoprotein recombination with porphyrins and hemes suggest that this lack of activity is a result of Fe-L5 bond breaking.
  • Slow heme transfer from horseradish peroxidases C2 and A2, cytochrome c peroxidase, chloroperoxidase, and leghemoglobins to a heme acceptor protein, apomyoglobin, has been studied under mild conditions. The reaction is best described as heme release into water followed by quick engulfment by apomyoglobin. The energetics of the activated process are large and interpreted as connected to both polypeptide motions during release and the ordering of water around the heme during solvation. The free energy required to break the iron(III)-ligand 5 (L5) bond is a minor but crucial portion of the activation free energy. Donor-acceptor protein interactions are not involved in the transfer. Fast heme release from inactive protein has also been observed. Apoprotein recombination with porphyrins and hemes suggest that this lack of activity is a result of Fe-L5 bond breaking.

Subject headings

NATURVETENSKAP  -- Fysik -- Annan fysik (hsv//swe)
NATURAL SCIENCES  -- Physical Sciences -- Other Physics Topics (hsv//eng)

Keyword

Fysik
Physics

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art (subject category)

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Smith, M.L.
Paul, Jan
Ohlsson, P.I.
Hjortsberg, K.
Paul, K.G.
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NATURAL SCIENCES
NATURAL SCIENCES
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and Other Physics To ...
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Luleå University of Technology

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